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Neil J. Oldham
Researcher at University of Nottingham
Publications - 128
Citations - 7584
Neil J. Oldham is an academic researcher from University of Nottingham. The author has contributed to research in topics: Mass spectrometry & Hypoxia-inducible factors. The author has an hindex of 43, co-authored 125 publications receiving 7032 citations. Previous affiliations of Neil J. Oldham include Miami University & Coventry University.
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Journal ArticleDOI
Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family
Kirsty S. Hewitson,Luke A McNeill,Madeline V. Riordan,Ya-Min Tian,Alex N. Bullock,Richard W.D. Welford,Jonathan M. Elkins,Neil J. Oldham,Shoumo Bhattacharya,Jonathan M. Gleadle,Peter J. Ratcliffe,Christopher W. Pugh,Christopher J. Schofield +12 more
TL;DR: Assays using recombinant FIH and HIF-α fragments revealed that FIH is the enzyme that hydroxylates the CAD asparagine residue, that the activity is directly inhibited by cobalt(II) and limited by hypoxia, and that the oxygen in the alcohol of the hydroxyasparagine residues is directly derived from dioxygen.
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Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).
Michael A. McDonough,Vivian S. W. Li,Emily Flashman,Rasheduzzaman Chowdhury,Christopher Mohr,Benoît M. R. Liénard,James Zondlo,Neil J. Oldham,Ian J. Clifton,Jeffrey Lewis,Luke A. McNeill,Robert J.M. Kurzeja,Kirsty S. Hewitson,Evelyn Yang,Steven R. Jordan,Rashid Syed,Christopher J. Schofield +16 more
TL;DR: The structure of the catalytic domain of human PHD2 provides insights into the hypoxic response, helps to rationalize a clinically observed mutation leading to familial erythrocytosis, and will aid in the design of PHD selective inhibitors for the treatment of anemia and ischemic disease.
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Expanding the diversity of chemical protein modification allows post-translational mimicry.
Sander I. van Kasteren,Holger B. Kramer,Henrik H. Jensen,Sandra J. Campbell,Joanna M. Kirkpatrick,Neil J. Oldham,Daniel C. Anthony,Benjamin G. Davis +7 more
TL;DR: A chemical tagging approach that enables the attachment of multiple modifications to bacterially expressed (bare) protein scaffolds allows reconstitution of functionally effective mimics of higher organism PTMs, and creates protein probes that included sensitive systems for detection of mammalian brain inflammation and disease.
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Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides
Michael F. Freeman,Cristian Gurgui,Maximilian J. Helf,Brandon I. Morinaka,Agustinus Robert Uria,Neil J. Oldham,Hans-Georg Sahl,Shigeki Matsunaga,Jörn Piel,Jörn Piel +9 more
TL;DR: A ribosomal origin is demonstrated of the marine sponge–derived polytheonamides, exceptionally potent, giant natural-product toxins, which broadens the biosynthetic scope of ribosomally synthesized peptides and proteins and creates new opportunities for peptide and protein bioengineering.
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Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)
Matthew E. Cockman,David E. Lancaster,Ineke P. Stolze,Kirsty S. Hewitson,Michael A. McDonough,Mathew L. Coleman,C.H. Coles,Xiaohong Yu,Ronald T. Hay,Steven C. Ley,Christopher W. Pugh,Neil J. Oldham,Norma Masson,Christopher J. Schofield,Peter J. Ratcliffe +14 more
TL;DR: It is shown that the human HIF asparaginyl hydroxylase, factor inhibiting HIF (FIH), also efficiently hydroxymates specific asparagsinyl (Asn)-residues within proteins of the IκB family, suggesting that FIH-dependent ARD hydroxyation is a common occurrence and potentially providing an oxygen-sensitive signal to a diverse range of processes.